HSBP 1 Human
Description
Heat Shock Response Regulation
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HSBP1 binds to the active trimeric form of Heat Shock Factor 1 (HSF1), inhibiting its DNA-binding activity and repressing heat shock protein (HSP) gene transcription .
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Overexpression in mammalian cells reduces HSF1-mediated transactivation by ~5-fold, confirming its role as a negative feedback regulator .
WASH Complex Interaction
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HSBP1 promotes the assembly and stability of the WASH complex (Wiskott-Aldrich syndrome protein and SCAR homolog), which regulates actin polymerization and endosomal trafficking .
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Depletion of HSBP1 disrupts WASH function, leading to defects in:
In Vitro Studies
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Thermal Stability: HSBP1 mutants (e.g., S31I) exhibit enhanced resistance to denaturation, suggesting engineered variants could improve industrial protein stability .
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Fluorescence Properties: Trp residues in HSBP1 mutants (R127W, S135F) show increased solvent exposure, aiding structural studies .
Cellular Mechanisms
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Cancer Biology: HSBP1 knockdown in cancer cells reduces metastatic potential by impairing focal adhesion turnover and directional migration .
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Neurological Protection: While HSBP1 itself is not directly neuroprotective, related sHSPs (e.g., HSPB1/Hsp27) mitigate tau aggregation in Alzheimer’s models .
Clinical and Industrial Relevance
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Therapeutic Target: HSBP1’s role in stress response and cancer metastasis highlights potential for targeting HSF1-HSBP1 interactions in hyperproliferative diseases .
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Biotechnological Use: Recombinant HSBP1 (Catalog #HSP-001) is utilized in laboratory research for studying protein-protein interactions and stress response pathways .
References
Product Specs
MAETDPKTVQ DLTSVVQTLL QQMQDKFQTM SDQIIGRIDD MSSRIDDLEK NIADLMTQAG VEELESENKI PATQKS.
Product Science Overview
Heat Shock Factor Binding Protein 1 (HSBP1) is a protein that plays a crucial role in the regulation of the heat shock response. This response is a cellular defense mechanism against stress conditions such as elevated temperatures, toxins, and other environmental stressors. HSBP1 is known to interact with Heat Shock Factor 1 (HSF1), a transcription factor that activates the expression of heat shock proteins (HSPs) which help in protein folding and protection against stress-induced damage .
HSBP1 is a small protein consisting of 76 amino acids. It is predominantly localized in the nucleus and interacts with the active trimeric state of HSF1. HSF1, in its inactive form, exists as a monomer with low affinity for DNA. Upon exposure to stress, HSF1 undergoes a conformational change to form an active trimer that binds to heat shock elements (HSEs) in the promoters of heat shock genes, thereby inducing their transcription .
HSBP1 acts as a negative regulator of HSF1. It binds to the trimeric form of HSF1 and inhibits its DNA-binding activity, thereby modulating the heat shock response. Overexpression of HSBP1 in mammalian cells has been shown to repress the transactivation activity of HSF1, indicating its role in fine-tuning the cellular response to stress .
The heat shock response is essential for cellular homeostasis and survival under stress conditions. HSBP1, by regulating HSF1 activity, ensures that the heat shock response is appropriately controlled. This regulation is crucial not only during stress but also in normal physiological conditions such as development, metabolism, and aging .
Recent studies have highlighted the broader role of HSF1 beyond the heat shock response. HSF1 is involved in various cellular processes, including metabolism, gametogenesis, and aging. Its dysregulation has been implicated in several pathologies, including cancer progression . Therefore, understanding the function and regulation of HSBP1 is important for comprehending the complex network of cellular stress responses and their implications in health and disease.
Recombinant HSBP1 refers to the protein produced through recombinant DNA technology, which involves inserting the gene encoding HSBP1 into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein can be used in various research applications to study its function, interactions, and regulatory mechanisms.
